Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil

• Published in: Anais da Academia Brasileira de Ciências 2015-03, Vol.87 (1), p.109-119
• Main Authors: Santos, Anderson F, Pires, Fabiano, Jesus, Hugo E, Santos, André L S, Peixoto, Raquel, Rosado, Alexandre S, D'Avila-Levy, Claudia M, Branquinha, Marta H
• Format: Article
• Language: English
• Subjects: Algoriphagus antarcticus; Antarctic Regions; Antártica; Bacterial Typing Techniques; Bacteroidetes - classification; Bacteroidetes - enzymology; Electrophoresis, Polyacrylamide Gel; Molecular Weight; MULTIDISCIPLINARY SCIENCES; Peptide Hydrolases - genetics; Peptide Hydrolases - isolation & purification; Phylogeny; Protease; Soil Microbiology; Sporosarcina - classification; Sporosarcina - enzymology; Sporosarcina aquimarina
• ISSN: 0001-3765; 1678-2690; 1678-2690; 0001-3765
• DOI: 10.1590/0001-3765201520130519

Two psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus (99%), with query coverage of 99% and 98%, respectively. The spent culture media from both isolates displayed proteolytic activities detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis containing gelatin as protein substrate. Under the employed conditions, S. aquimarina showed a 55 kDa protease with the best activity detected at pH 7.0 and at 27°C. A. antarcticus also showed a single extracellular protease, however its molecular mass was around 90kDa and its best activity was detected at pH 9.0 and at 37°C. The proteases from both isolates were inhibited by 1,10-phenanthroline and EDTA, two metalloprotease inhibitors. This is the first record of protease detection in both species, and our results may contribute to broaden the basic knowledge of proteases from the Antarctica environment and may help prospecting future biotechnological applications of these enzymes.